ID   SRTX2_ATRIR             Reviewed;         118 AA.
AC   P0DJK1;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Sarafotoxin-i2;
DE            Short=SRTX-i2;
DE   Flags: Precursor;
OS   Atractaspis irregularis (Variable burrowing asp) (Elaps irregularis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Lamprophiidae; Atractaspidinae; Atractaspis.
OX   NCBI_TaxID=512568;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16223250; DOI=10.1021/ac050575k;
RA   Quinton L., Le Caer J.P., Phan G., Ligny-Lemaire C., Bourdais-Jomaron J.,
RA   Ducancel F., Chamot-Rooke J.;
RT   "Characterization of toxins within crude venoms by combined use of Fourier
RT   transform mass spectrometry and cloning.";
RL   Anal. Chem. 77:6630-6639(2005).
CC   -!- FUNCTION: Vasoconstrictor activity. These toxins cause cardiac arrest
CC       probably as a result of coronary vasospasm. Acts by displaying
CC       agonistic activities towards endothelin-1 and -2 receptors (EDNRA and
CC       EDNRB) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Different length molecules ranging from 17 (85-101) to 30 amino
CC       acids (85-114) have been found in the venom.
CC       {ECO:0000269|PubMed:16223250}.
CC   -!- MASS SPECTROMETRY: Mass=2950.1; Method=Electrospray; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:16223250};
CC   -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DJK1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR   InterPro; IPR019764; Endothelin_toxin_CS.
DR   InterPro; IPR001928; Endothln-like_toxin.
DR   Pfam; PF00322; Endothelin; 1.
DR   SMART; SM00272; END; 1.
DR   PROSITE; PS00270; ENDOTHELIN; 1.
PE   1: Evidence at protein level;
KW   Cardiotoxin; Cleavage on pair of basic residues; Disulfide bond;
KW   G-protein coupled receptor impairing toxin; Secreted; Signal; Toxin;
KW   Vasoactive; Vasoconstrictor.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..84
FT                   /id="PRO_0000421167"
FT   PEPTIDE         85..109
FT                   /note="Sarafotoxin-i2"
FT                   /id="PRO_0000421168"
FT   PROPEP          112..118
FT                   /id="PRO_0000421169"
FT   SITE            105
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        85..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   118 AA;  12718 MW;  4E4F859E40E5002E CRC64;
     MALLPRLAAG GLLLLMALAA LDGKPAPPKL LQKLMDGGQR RSEDQAAAGR IIDYEDGDEP
     VAVSVGDTKQ AARALSPLRK PQPLCSCADM SDLECMNFCR LDVMWVNRNR KPSPIQSS